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Visualizing the analogy between competitive adsorption and colloid stability to restore lung surfactant function.

Abstract
We investigated a model of acute respiratory distress syndrome in which the serum protein albumin adsorbs to an air-liquid interface and prevents the thermodynamically preferable adsorption of the clinical lung surfactant Survanta by inducing steric and electrostatic energy barriers analogous to those that prevent colloidal aggregation. Chitosan and polyethylene glycol (PEG), two polymers that traditionally have been used to aggregate colloids, both allow Survanta to quantitatively displace albumin from the interface, but through two distinct mechanisms. Direct visualization with confocal microscopy shows that the polycation chitosan coadsorbs to interfacial layers of both Survanta and albumin, and also colocalizes with the anionic domains of Survanta at the air-liquid interface, consistent with it eliminating the electrostatic repulsion by neutralizing the surface charges on albumin and Survanta. In contrast, the PEG distribution does not change during the displacement of albumin by Survanta, consistent with PEG inducing a depletion attraction sufficient to overcome the repulsive energy barrier toward adsorption.
AuthorsIan C Shieh, Alan J Waring, Joseph A Zasadzinski
JournalBiophysical journal (Biophys J) Vol. 102 Issue 4 Pg. 777-86 (Feb 22 2012) ISSN: 1542-0086 [Electronic] United States
PMID22385848 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
CopyrightCopyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Chemical References
  • Biological Products
  • Colloids
  • Pulmonary Surfactants
  • Serum Albumin, Bovine
  • Polyethylene Glycols
  • Chitosan
  • beractant
Topics
  • Adsorption
  • Animals
  • Biological Products (chemistry, pharmacology)
  • Cattle
  • Chitosan (chemistry)
  • Colloids
  • Microscopy, Confocal
  • Polyethylene Glycols (chemistry)
  • Pulmonary Surfactants (chemistry, pharmacology)
  • Serum Albumin, Bovine (chemistry)
  • Spectrometry, Fluorescence
  • Surface Properties

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